Abstract

Tropomyosin (Tm) oscillates periodically between three equilibrium states over the surface of actin filament during the cardiac thin filament activation process. This motion has shown to be essential in regulating the access of Myosin heads to actin binding sites, hence the cross-bridge cycling dynamics. Since the trajectory landscape of Tm motions depends critically on its micromechanical characteristics represented primarily by its stiffness or rigidity. It is important to study the effects of Tm stiffness variations on the sarcomere contraction.

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